| http://purl.uniprot.org/citations/15385955 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15385955 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15385955 | http://www.w3.org/2000/01/rdf-schema#comment | "An interferon-induced endoribonuclease, ribonuclease L (RNase L), is implicated in both the molecular mechanism of action of interferon and the fundamental control of RNA stability in mammalian cells. RNase L is catalytically active only after binding to an unusual activator molecule containing a 5'-phosphorylated 2',5'-linked oligoadenylate (2-5A), in the N-terminal half. Here, we report the crystal structure of the N-terminal ankyrin repeat domain (ANK) of human RNase L complexed with the activator 2-5A. This is the first structural view of an ankyrin repeat structure directly interacting with a nucleic acid, rather than with a protein. The ANK domain folds into eight ankyrin repeat elements and forms an extended curved structure with a concave surface. The 2-5A molecule is accommodated at a concave site and directly interacts with ankyrin repeats 2-4. Interestingly, two structurally equivalent 2-5A binding motifs are found at repeats 2 and 4. The structural basis for 2-5A recognition by ANK is essential for designing stable 2-5As with a high likelihood of activating RNase L."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600420"xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600420"xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Goto Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Goto Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Kitade Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Kitade Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Nakanishi M."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Nakanishi M."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Tanaka N."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Tanaka N."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Kusakabe Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Kusakabe Y."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Nakamura K.T."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/author | "Nakamura K.T."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/pages | "3929-3938"xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/pages | "3929-3938"xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/title | "Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L."xsd:string |
| http://purl.uniprot.org/citations/15385955 | http://purl.uniprot.org/core/title | "Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L."xsd:string |